TRIPC_HUMAN - dbPTM
TRIPC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRIPC_HUMAN
UniProt AC Q14669
Protein Name E3 ubiquitin-protein ligase TRIP12
Gene Name TRIP12
Organism Homo sapiens (Human).
Sequence Length 1992
Subcellular Localization Nucleus, nucleoplasm .
Protein Description E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes..
Protein Sequence MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPKALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPESNQEAVNSSAARTDEAPQGAAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEQINEDTGTARAIQRKPNPLANSNTSGYSESKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSMGSTTSVSSGTATAATHAAADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSTQSNSNNIEPARTAGGSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPIGRVEPVGNAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGTGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSIQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESNKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVSNPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQQSFHLS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSNRPNNNP
------CCCCCCCCC
53.5021406692
12PhosphorylationPNNNPGGSLRRSQRN
CCCCCCCCCCHHHCC
25.3123401153
34PhosphorylationDDSIGGRSCSSSSAV
CCCCCCCCCCCCCCE
22.9421712546
36PhosphorylationSIGGRSCSSSSAVIV
CCCCCCCCCCCCEEE
34.2024719451
38PhosphorylationGGRSCSSSSAVIVPQ
CCCCCCCCCCEEECC
13.1628555341
44 (in isoform 3)Phosphorylation-32.6530266825
45 (in isoform 3)Phosphorylation-43.0230266825
49 (in isoform 3)Phosphorylation-31.1830266825
52 (in isoform 3)Phosphorylation-30.91-
54PhosphorylationEDPDRANTSERQKTG
CCCCCCCCCHHHHCC
30.8628555341
54 (in isoform 3)Phosphorylation-30.86-
75PhosphorylationNSRGVKRSASPDYNR
CCCCCCCCCCCCCCC
27.6430266825
77PhosphorylationRGVKRSASPDYNRTN
CCCCCCCCCCCCCCC
21.3929255136
80PhosphorylationKRSASPDYNRTNSPS
CCCCCCCCCCCCCCC
15.2130266825
83PhosphorylationASPDYNRTNSPSSAK
CCCCCCCCCCCCCCC
36.0925159151
85PhosphorylationPDYNRTNSPSSAKKP
CCCCCCCCCCCCCCC
26.0825159151
87PhosphorylationYNRTNSPSSAKKPKA
CCCCCCCCCCCCCCC
42.6322617229
88PhosphorylationNRTNSPSSAKKPKAL
CCCCCCCCCCCCCCC
47.7121955146
90 (in isoform 4)Phosphorylation-72.1218669648
98PhosphorylationKPKALQHTESPSETN
CCCCCCCCCCCCCCC
25.7929255136
100PhosphorylationKALQHTESPSETNKP
CCCCCCCCCCCCCCC
34.5823401153
102PhosphorylationLQHTESPSETNKPHS
CCCCCCCCCCCCCCC
67.3530266825
104PhosphorylationHTESPSETNKPHSKS
CCCCCCCCCCCCCHH
53.5329255136
109PhosphorylationSETNKPHSKSKKRHL
CCCCCCCCHHHHHHC
47.3425159151
111PhosphorylationTNKPHSKSKKRHLDQ
CCCCCCHHHHHHCCH
46.5626434776
123MethylationLDQEQQLKSAQSPST
CCHHHHHHHCCCCCC
39.13115979483
127PhosphorylationQQLKSAQSPSTSKAH
HHHHHCCCCCCCCHH
22.1224719451
129PhosphorylationLKSAQSPSTSKAHTR
HHHCCCCCCCCHHHH
51.0328176443
130PhosphorylationKSAQSPSTSKAHTRK
HHCCCCCCCCHHHHC
37.3228985074
148AcetylationTGGSRSQKRKRTESS
CCCCHHHHCCCCCCC
62.2219822159
152PhosphorylationRSQKRKRTESSCVKS
HHHHCCCCCCCCCCC
43.16-
155PhosphorylationKRKRTESSCVKSGSG
HCCCCCCCCCCCCCC
19.3930576142
159PhosphorylationTESSCVKSGSGSEST
CCCCCCCCCCCCCCC
20.1425850435
161PhosphorylationSSCVKSGSGSESTGA
CCCCCCCCCCCCCCC
46.3529255136
163PhosphorylationCVKSGSGSESTGAEE
CCCCCCCCCCCCCCH
30.0325850435
165PhosphorylationKSGSGSESTGAEERS
CCCCCCCCCCCCHHC
33.5625056879
166PhosphorylationSGSGSESTGAEERSA
CCCCCCCCCCCHHCC
36.0426074081
181AcetylationKPTKLASKSATSAKA
CCCCHHCCCCCCCCC
38.2025953088
192PhosphorylationSAKAGCSTITDSSSA
CCCCCCCCCCCCCCC
31.79-
194PhosphorylationKAGCSTITDSSSAAS
CCCCCCCCCCCCCCC
29.89-
214PhosphorylationSAVASASSTVPPGAR
CCHHHCCCCCCCCCC
32.8924260401
223MethylationVPPGARVKQGKDQNK
CCCCCCCCCCCCCHH
48.02116252675
234PhosphorylationDQNKARRSRSASSPS
CCHHHHHHHCCCCCC
25.6523403867
236PhosphorylationNKARRSRSASSPSPR
HHHHHHHCCCCCCCC
33.4828258704
238PhosphorylationARRSRSASSPSPRRS
HHHHHCCCCCCCCCC
43.9923403867
239PhosphorylationRRSRSASSPSPRRSS
HHHHCCCCCCCCCCH
29.1628176443
241PhosphorylationSRSASSPSPRRSSRE
HHCCCCCCCCCCHHH
32.7428176443
245PhosphorylationSSPSPRRSSREKEQS
CCCCCCCCHHHHHHH
34.7226074081
246PhosphorylationSPSPRRSSREKEQSK
CCCCCCCHHHHHHHC
42.5226074081
259AcetylationSKTGGSSKFDWAARF
HCCCCCCCCCHHHHC
49.3825953088
259UbiquitinationSKTGGSSKFDWAARF
HCCCCCCCCCHHHHC
49.38-
267PhosphorylationFDWAARFSPKVSLPK
CCHHHHCCCCCCCCC
20.4725159151
271PhosphorylationARFSPKVSLPKTKLS
HHCCCCCCCCCCCCC
45.1130576142
276AcetylationKVSLPKTKLSLPGSS
CCCCCCCCCCCCCCC
42.0525953088
276UbiquitinationKVSLPKTKLSLPGSS
CCCCCCCCCCCCCCC
42.05-
278PhosphorylationSLPKTKLSLPGSSKS
CCCCCCCCCCCCCCC
33.7925159151
282PhosphorylationTKLSLPGSSKSETSK
CCCCCCCCCCCCCCC
32.4320068231
283PhosphorylationKLSLPGSSKSETSKP
CCCCCCCCCCCCCCC
46.2220068231
285PhosphorylationSLPGSSKSETSKPGP
CCCCCCCCCCCCCCC
48.3220068230
287PhosphorylationPGSSKSETSKPGPSG
CCCCCCCCCCCCCCH
49.49-
288PhosphorylationGSSKSETSKPGPSGL
CCCCCCCCCCCCCHH
32.57-
289UbiquitinationSSKSETSKPGPSGLQ
CCCCCCCCCCCCHHH
62.50-
293PhosphorylationETSKPGPSGLQAKLA
CCCCCCCCHHHHHHH
59.0424114839
298AcetylationGPSGLQAKLASLRKS
CCCHHHHHHHHHHHH
31.4625953088
298UbiquitinationGPSGLQAKLASLRKS
CCCHHHHHHHHHHHH
31.4621906983
298UbiquitinationGPSGLQAKLASLRKS
CCCHHHHHHHHHHHH
31.4621890473
301PhosphorylationGLQAKLASLRKSTKK
HHHHHHHHHHHHCCC
38.8624719451
305PhosphorylationKLASLRKSTKKRSES
HHHHHHHHCCCCCCC
38.7426434776
306PhosphorylationLASLRKSTKKRSESP
HHHHHHHCCCCCCCC
43.5526434776
308MethylationSLRKSTKKRSESPPA
HHHHHCCCCCCCCCC
62.33116252683
310PhosphorylationRKSTKKRSESPPAEL
HHHCCCCCCCCCCCC
51.8329255136
312PhosphorylationSTKKRSESPPAELPS
HCCCCCCCCCCCCCH
37.1119664994
319PhosphorylationSPPAELPSLRRSTRQ
CCCCCCCHHHHCCCC
47.3230266825
327UbiquitinationLRRSTRQKTTGSCAS
HHHCCCCCCCCCCCC
44.77-
328O-linked_GlycosylationRRSTRQKTTGSCAST
HHCCCCCCCCCCCCC
28.22OGP
329O-linked_GlycosylationRSTRQKTTGSCASTS
HCCCCCCCCCCCCCC
33.85OGP
329PhosphorylationRSTRQKTTGSCASTS
HCCCCCCCCCCCCCC
33.8520068230
331O-linked_GlycosylationTRQKTTGSCASTSRR
CCCCCCCCCCCCCCC
12.38OGP
331PhosphorylationTRQKTTGSCASTSRR
CCCCCCCCCCCCCCC
12.3820068230
334PhosphorylationKTTGSCASTSRRGSG
CCCCCCCCCCCCCCC
31.1030576142
340PhosphorylationASTSRRGSGLGKRGA
CCCCCCCCCCCHHHH
29.0930576142
340UbiquitinationASTSRRGSGLGKRGA
CCCCCCCCCCCHHHH
29.0921890473
355UbiquitinationAEARRQEKMADPESN
HHHHHHHHHCCCCHH
30.9321906983
356SulfoxidationEARRQEKMADPESNQ
HHHHHHHHCCCCHHH
5.1421406390
361PhosphorylationEKMADPESNQEAVNS
HHHCCCCHHHHHHHH
49.56-
369PhosphorylationNQEAVNSSAARTDEA
HHHHHHHHHCCCCCC
22.27-
373PhosphorylationVNSSAARTDEAPQGA
HHHHHCCCCCCCCCC
33.2024043423
387PhosphorylationAAGAVGMTTSGESES
CCCCCCCCCCCCCCC
16.3318669648
388PhosphorylationAGAVGMTTSGESESD
CCCCCCCCCCCCCCC
26.3324043423
389PhosphorylationGAVGMTTSGESESDD
CCCCCCCCCCCCCCC
31.2524043423
392PhosphorylationGMTTSGESESDDSEM
CCCCCCCCCCCCCHH
46.0224043423
393 (in isoform 2)Phosphorylation-54.6118669648
394PhosphorylationTTSGESESDDSEMGR
CCCCCCCCCCCHHHH
56.8724043423
397PhosphorylationGESESDDSEMGRLQA
CCCCCCCCHHHHHHH
34.1827251789
422MethylationLFGPLGPRMSQLFHR
HCCCCCHHHHHHHHH
35.2754560333
424PhosphorylationGPLGPRMSQLFHRTI
CCCCHHHHHHHHHHH
25.6323401153
435 (in isoform 3)Phosphorylation-16.6018669648
507PhosphorylationHACRALTYMMEALPR
HHHHHHHHHHHHCCC
8.7017053785
515PhosphorylationMMEALPRSSAVVVDA
HHHHCCCCCCCCCCC
22.2523403867
516PhosphorylationMEALPRSSAVVVDAI
HHHCCCCCCCCCCCH
26.7723403867
617MalonylationRLTHQDKKSVESTCL
HCCCCCHHHHHHHHH
68.9426320211
617UbiquitinationRLTHQDKKSVESTCL
HCCCCCHHHHHHHHH
68.94-
650PhosphorylationVASKDLLTNVQQLLV
HHCHHHHHHHHHHHH
40.41-
748PhosphorylationEGIFAVDTMLKKGNA
CCEEEHHHHHHCCCC
20.1525850435
751UbiquitinationFAVDTMLKKGNAQNT
EEHHHHHHCCCCCCC
48.05-
752UbiquitinationAVDTMLKKGNAQNTD
EHHHHHHCCCCCCCC
54.13-
758PhosphorylationKKGNAQNTDGAIWQW
HCCCCCCCCCCCEEE
24.5920068231
768UbiquitinationAIWQWRDDRGLWHPY
CCEEEECCCCCCCCC
37.6621890473
768UbiquitinationAIWQWRDDRGLWHPY
CCEEEECCCCCCCCC
37.6621890473
778UbiquitinationLWHPYNRIDSRIIEQ
CCCCCCCCCHHHHHH
5.1321890473
778UbiquitinationLWHPYNRIDSRIIEQ
CCCCCCCCCHHHHHH
5.1321890473
780PhosphorylationHPYNRIDSRIIEQIN
CCCCCCCHHHHHHHH
24.0224247654
792PhosphorylationQINEDTGTARAIQRK
HHHCCCCCHHHHHCC
18.31-
799UbiquitinationTARAIQRKPNPLANS
CHHHHHCCCCCCCCC
32.5421906983
809PhosphorylationPLANSNTSGYSESKK
CCCCCCCCCCCCCHH
39.7328555341
811PhosphorylationANSNTSGYSESKKDD
CCCCCCCCCCCHHHH
14.7225839225
815UbiquitinationTSGYSESKKDDARAQ
CCCCCCCHHHHHHHH
57.05-
825UbiquitinationDARAQLMKEDPELAK
HHHHHHHHHCHHHHH
68.50-
832UbiquitinationKEDPELAKSFIKTLF
HHCHHHHHHHHHHHH
59.53-
833PhosphorylationEDPELAKSFIKTLFG
HCHHHHHHHHHHHHH
26.9624719451
936PhosphorylationQVKHLAESESLLTSP
HHHHHHHCHHHCCCC
27.2125867546
938PhosphorylationKHLAESESLLTSPPK
HHHHHCHHHCCCCCC
37.6525867546
941PhosphorylationAESESLLTSPPKACT
HHCHHHCCCCCCCCC
44.4730266825
942PhosphorylationESESLLTSPPKACTN
HCHHHCCCCCCCCCC
38.8929255136
953PhosphorylationACTNGSGSMGSTTSV
CCCCCCCCCCCCCCC
22.9730576142
977PhosphorylationHAAADLGSPSLQHSR
HHHHHCCCCCCCCCC
20.7230576142
979PhosphorylationAADLGSPSLQHSRDD
HHHCCCCCCCCCCCC
42.2126074081
983PhosphorylationGSPSLQHSRDDSLDL
CCCCCCCCCCCCCCC
25.1726074081
987PhosphorylationLQHSRDDSLDLSPQG
CCCCCCCCCCCCCCC
28.2430266825
989UbiquitinationHSRDDSLDLSPQGRL
CCCCCCCCCCCCCCH
49.4021890473
989UbiquitinationHSRDDSLDLSPQGRL
CCCCCCCCCCCCCCH
49.4021890473
991PhosphorylationRDDSLDLSPQGRLSD
CCCCCCCCCCCCHHH
18.1629255136
997PhosphorylationLSPQGRLSDVLKRKR
CCCCCCHHHHHHHCC
25.0623401153
1001UbiquitinationGRLSDVLKRKRLPKR
CCHHHHHHHCCCCCC
56.5821906983
1015PhosphorylationRGPRRPKYSPPRDDD
CCCCCCCCCCCCCCC
29.1430266825
1016PhosphorylationGPRRPKYSPPRDDDK
CCCCCCCCCCCCCCC
34.2629255136
1018UbiquitinationRRPKYSPPRDDDKVD
CCCCCCCCCCCCCCC
46.5221890473
1018UbiquitinationRRPKYSPPRDDDKVD
CCCCCCCCCCCCCCC
46.5221890473
1029UbiquitinationDKVDNQAKSPTTTQS
CCCCCCCCCCCCCCC
47.40-
1030PhosphorylationKVDNQAKSPTTTQSP
CCCCCCCCCCCCCCC
30.4123401153
1032PhosphorylationDNQAKSPTTTQSPKS
CCCCCCCCCCCCCCH
49.9523927012
1033PhosphorylationNQAKSPTTTQSPKSS
CCCCCCCCCCCCCHH
26.6523927012
1034PhosphorylationQAKSPTTTQSPKSSF
CCCCCCCCCCCCHHH
29.5423927012
1036PhosphorylationKSPTTTQSPKSSFLA
CCCCCCCCCCHHHHH
32.0023927012
1038UbiquitinationPTTTQSPKSSFLASL
CCCCCCCCHHHHHHC
65.0721906983
1038UbiquitinationPTTTQSPKSSFLASL
CCCCCCCCHHHHHHC
65.0721890473
1039PhosphorylationTTTQSPKSSFLASLN
CCCCCCCHHHHHHCC
29.7026074081
1040PhosphorylationTTQSPKSSFLASLNP
CCCCCCHHHHHHCCC
30.3326074081
1044PhosphorylationPKSSFLASLNPKTWG
CCHHHHHHCCCCCCC
30.7225159151
1048UbiquitinationFLASLNPKTWGRLST
HHHHCCCCCCCCCCC
56.7021906983
1048UbiquitinationFLASLNPKTWGRLST
HHHHCCCCCCCCCCC
56.7021890473
1049PhosphorylationLASLNPKTWGRLSTQ
HHHCCCCCCCCCCCC
34.1122199227
1054PhosphorylationPKTWGRLSTQSNSNN
CCCCCCCCCCCCCCC
24.0429255136
1055PhosphorylationKTWGRLSTQSNSNNI
CCCCCCCCCCCCCCC
40.3829255136
1057PhosphorylationWGRLSTQSNSNNIEP
CCCCCCCCCCCCCCC
42.1729255136
1059PhosphorylationRLSTQSNSNNIEPAR
CCCCCCCCCCCCCCH
36.1829255136
1067PhosphorylationNNIEPARTAGGSGLA
CCCCCCHHCCCCHHH
31.59-
1078PhosphorylationSGLARAASKDTISNN
CHHHHHHCCCCHHCC
30.0423401153
1079UbiquitinationGLARAASKDTISNNR
HHHHHHCCCCHHCCH
54.91-
1081PhosphorylationARAASKDTISNNREK
HHHHCCCCHHCCHHH
30.0027794612
1083PhosphorylationAASKDTISNNREKIK
HHCCCCHHCCHHHHH
30.0926270265
1086UbiquitinationKDTISNNREKIKGWI
CCCHHCCHHHHHHHH
51.3321890473
1096UbiquitinationIKGWIKEQAHKFVER
HHHHHHHHHHHHHHH
43.7121890473
1104PhosphorylationAHKFVERYFSSENMD
HHHHHHHHHCCCCCC
8.3625850435
1106PhosphorylationKFVERYFSSENMDGS
HHHHHHHCCCCCCCC
28.0125850435
1107PhosphorylationFVERYFSSENMDGSN
HHHHHHCCCCCCCCC
24.0825850435
1113PhosphorylationSSENMDGSNPALNVL
CCCCCCCCCHHHHHH
35.0625850435
1146PhosphorylationECLVEIRSIVSESDV
EEEEEEHHEECCCCC
32.7623898821
1149PhosphorylationVEIRSIVSESDVSSF
EEEHHEECCCCCCCE
29.7023898821
1151PhosphorylationIRSIVSESDVSSFEI
EHHEECCCCCCCEEE
35.4923898821
1154PhosphorylationIVSESDVSSFEIQHS
EECCCCCCCEEEECC
34.0123898821
1155PhosphorylationVSESDVSSFEIQHSG
ECCCCCCCEEEECCH
27.0923898821
1161PhosphorylationSSFEIQHSGFVKQLL
CCEEEECCHHHHHHH
19.9723898821
1170PhosphorylationFVKQLLLYLTSKSEK
HHHHHHHHHHCCCHH
14.1123898821
1172PhosphorylationKQLLLYLTSKSEKDA
HHHHHHHHCCCHHHH
22.1323898821
1173PhosphorylationQLLLYLTSKSEKDAV
HHHHHHHCCCHHHHH
31.4323898821
1174UbiquitinationLLLYLTSKSEKDAVS
HHHHHHCCCHHHHHH
58.35-
1177UbiquitinationYLTSKSEKDAVSREI
HHHCCCHHHHHHHHH
59.06-
1221UbiquitinationPLLALVHKMNNCLSQ
HHHHHHHHHHHHHHH
35.52-
1241PhosphorylationVKVHDFPSGNGTGGS
CEEECCCCCCCCCCC
44.9028450419
1245PhosphorylationDFPSGNGTGGSFSLN
CCCCCCCCCCCCCCC
42.2328450419
1248PhosphorylationSGNGTGGSFSLNRGS
CCCCCCCCCCCCCCC
17.0128450419
1250PhosphorylationNGTGGSFSLNRGSQA
CCCCCCCCCCCCCHH
26.8228450419
1259UbiquitinationNRGSQALKFFNTHQL
CCCCHHHHHCCHHHH
51.4221890473
1259UbiquitinationNRGSQALKFFNTHQL
CCCCHHHHHCCHHHH
51.4221890473
1267AcetylationFFNTHQLKCQLQRHP
HCCHHHHHHHHHCCC
17.2325953088
1267UbiquitinationFFNTHQLKCQLQRHP
HCCHHHHHHHHHCCC
17.23-
1280AcetylationHPDCANVKQWKGGPV
CCCCCCCCCCCCCCC
50.6919816199
1280UbiquitinationHPDCANVKQWKGGPV
CCCCCCCCCCCCCCC
50.69-
1283AcetylationCANVKQWKGGPVKID
CCCCCCCCCCCCCCC
52.0419816211
1283UbiquitinationCANVKQWKGGPVKID
CCCCCCCCCCCCCCC
52.04-
1288AcetylationQWKGGPVKIDPLALV
CCCCCCCCCCHHHHH
44.5223236377
1288UbiquitinationQWKGGPVKIDPLALV
CCCCCCCCCCHHHHH
44.5221890473
1288UbiquitinationQWKGGPVKIDPLALV
CCCCCCCCCCHHHHH
44.5221890473
1307UbiquitinationRYLVVRGYGRVREDD
HHHHHCCCCCCCCCC
7.3821890473
1317PhosphorylationVREDDEDSDDDGSDE
CCCCCCCCCCCCCHH
40.6726503892
1322PhosphorylationEDSDDDGSDEEIDES
CCCCCCCCHHHHHHH
49.1726503892
1329PhosphorylationSDEEIDESLAAQFLN
CHHHHHHHHHHHHHH
21.4028176443
1336UbiquitinationSLAAQFLNSGNVRHR
HHHHHHHHCCCHHHE
49.5121890473
1347PhosphorylationVRHRLQFYIGEHLLP
HHHEEEEEECCCCCC
8.6124043423
1355PhosphorylationIGEHLLPYNMTVYQA
ECCCCCCCCCHHHHH
19.9624043423
1358PhosphorylationHLLPYNMTVYQAVRQ
CCCCCCCHHHHHHHH
16.6624043423
1360PhosphorylationLPYNMTVYQAVRQFS
CCCCCHHHHHHHHHC
5.0024043423
1367PhosphorylationYQAVRQFSIQAEDER
HHHHHHHCCCCCCCC
12.8823927012
1374MethylationSIQAEDERESTDDES
CCCCCCCCCCCCCCC
56.33115918973
1376PhosphorylationQAEDERESTDDESNP
CCCCCCCCCCCCCCC
43.2726503892
1377PhosphorylationAEDERESTDDESNPL
CCCCCCCCCCCCCCC
42.5926503892
1381PhosphorylationRESTDDESNPLGRAG
CCCCCCCCCCCCCCC
51.2230266825
1399UbiquitinationKTHTIWYKPVREDEE
ECEEEEEECCCCCHH
23.26-
1421PhosphorylationGKRGRAQTAPTKTSP
CCCCCCCCCCCCCCC
33.3523927012
1424PhosphorylationGRAQTAPTKTSPRNA
CCCCCCCCCCCCCCH
44.4830266825
1425AcetylationRAQTAPTKTSPRNAK
CCCCCCCCCCCCCHH
46.04-
1425UbiquitinationRAQTAPTKTSPRNAK
CCCCCCCCCCCCCHH
46.04-
1426PhosphorylationAQTAPTKTSPRNAKK
CCCCCCCCCCCCHHC
46.5823401153
1427PhosphorylationQTAPTKTSPRNAKKH
CCCCCCCCCCCHHCC
24.3426846344
1500PhosphorylationMCKEIIPTSEFINSK
CCCHHCCHHHHHHHH
30.4021406692
1501PhosphorylationCKEIIPTSEFINSKL
CCHHCCHHHHHHHHH
25.7521406692
1506PhosphorylationPTSEFINSKLTAKAN
CHHHHHHHHHHHHHH
24.9921406692
1507UbiquitinationTSEFINSKLTAKANR
HHHHHHHHHHHHHHH
45.42-
1524PhosphorylationQDPLVIMTGNIPTWL
CCCEEEEECCCHHHH
18.8920068231
1529PhosphorylationIMTGNIPTWLTELGK
EEECCCHHHHHHHHC
29.3420068231
1532PhosphorylationGNIPTWLTELGKTCP
CCCHHHHHHHHCCCC
22.2620068231
1552PhosphorylationDTRQMLFYVTAFDRD
CHHHHEEEEEECCHH
7.9123663014
1554PhosphorylationRQMLFYVTAFDRDRA
HHHEEEEEECCHHHH
15.3823663014
1568PhosphorylationAMQRLLDTNPEINQS
HHHHHHHCCCCCCCC
53.2820873877
1575PhosphorylationTNPEINQSDSQDSRV
CCCCCCCCCCCCCCH
34.4429255136
1577PhosphorylationPEINQSDSQDSRVAP
CCCCCCCCCCCCHHH
40.9317525332
1580PhosphorylationNQSDSQDSRVAPRLD
CCCCCCCCCHHHHHC
22.4829255136
1592PhosphorylationRLDRKKRTVNREELL
HHCHHCCCCCHHHHH
30.8922817900
1600UbiquitinationVNREELLKQAESVMQ
CCHHHHHHHHHHHHH
61.1521906983
1661UbiquitinationEVTLSNPKGSQEGTK
EEECCCCCCCHHHHH
75.3721906983
1663PhosphorylationTLSNPKGSQEGTKYI
ECCCCCCCHHHHHHH
31.05-
1668UbiquitinationKGSQEGTKYIQNLQG
CCCHHHHHHHHHHHH
51.73-
1686UbiquitinationLPFGRTAKPAHIAKV
CCCCCCCCCHHHHHH
41.97-
1692UbiquitinationAKPAHIAKVKMKFRF
CCCHHHHHHHHHHHH
41.61-
1702UbiquitinationMKFRFLGKLMAKAIM
HHHHHHHHHHHHHHH
36.92-
1706UbiquitinationFLGKLMAKAIMDFRL
HHHHHHHHHHHHHCC
25.20-
1724UbiquitinationPLGLPFYKWMLRQET
CCCCCHHHHHHHCCC
26.89-
1766UbiquitinationKKRLEQDKSQTKESL
HHHHHHCHHHHHHHH
44.13-
1795PhosphorylationEDLGLDFTLPGFPNI
HHCCCCCCCCCCCCE
31.5426074081
1809UbiquitinationIELKKGGKDIPVTIH
EEECCCCEECCEEEC
62.24-
1814PhosphorylationGGKDIPVTIHNLEEY
CCEECCEEECCHHHH
15.9126074081
1840PhosphorylationGVSRQFDSFRDGFES
CHHHHCHHHHCCCHH
24.3822468782
1847PhosphorylationSFRDGFESVFPLSHL
HHHCCCHHCCCHHHH
27.1422468782
1852PhosphorylationFESVFPLSHLQYFYP
CHHCCCHHHHHHHCH
23.5322468782
1856PhosphorylationFPLSHLQYFYPEELD
CCHHHHHHHCHHHHH
16.0822468782
1877UbiquitinationKADTWDAKTLMECCR
CCCCCCHHHHHHHCC
39.45-
1937PhosphorylationRSLNPPLTIVRKTFE
CCCCCCEEEEEHHHC
24.17-
1941UbiquitinationPPLTIVRKTFESTEN
CCEEEEEHHHCCCCC
46.82-
1942PhosphorylationPLTIVRKTFESTENP
CEEEEEHHHCCCCCH
23.28-
1955PhosphorylationNPDDFLPSVMTCVNY
CHHCHHHHHHHHHHH
27.03-
1977UbiquitinationSIEIMREKLLIAARE
HHHHHHHHHHHHHHC
37.92-
1988PhosphorylationAAREGQQSFHLS---
HHHCCCCCCCCC---
13.5227499020

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1078SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRIPC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TRIPC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ULA1_HUMANNAE1physical
18627766
CDN2A_HUMANCDKN2Aphysical
20208519
ARF_HUMANCDKN2Aphysical
20208519
MYC_HUMANMYCphysical
20208519
TRADD_HUMANTRADDphysical
22561347
NMI_HUMANNMIphysical
23034180
CDN2A_HUMANCDKN2Aphysical
23034180
ARF_HUMANCDKN2Aphysical
23034180
UB2D1_HUMANUBE2D1physical
18627766
UB2D1_HUMANUBE2D1physical
9575161
UB2L3_HUMANUBE2L3physical
9575161
SOX6_HUMANSOX6physical
23663701
UB2D1_HUMANUBE2D1physical
23663701
GNL3_HUMANGNL3physical
24769896
UB2D1_HUMANUBE2D1physical
19028681
UBC_HUMANUBCphysical
19028681
PTF1A_HUMANPTF1Aphysical
25355311
UBP7_HUMANUSP7physical
27800609

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRIPC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-991; SER-1317AND SER-1322, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-312; SER-991;SER-997; SER-1317 AND SER-1322, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1577, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-88 AND SER-1427,AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND THR-1592, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-507, AND MASSSPECTROMETRY.

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